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Ubiquitin has intrinsic proteolytic activity: implications for cellular regulation.

V A Fried, H T Smith, E Hildebrandt

    Proceedings of the National Academy of Sciences of the United States of America
    |June 1, 1987
    PubMed
    Summary

    Ubiquitin, a protein in all eukaryotic cells, possesses intrinsic proteolytic activity, acting as a protease. This discovery redefines ubiquitin

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    Area of Science:

    • Molecular Biology
    • Biochemistry
    • Cell Biology

    Background:

    • Ubiquitin is a conserved protein found in all eukaryotic cells.
    • Its known roles include protein degradation and conjugation to cellular proteins.
    • The precise function of ubiquitin in cellular events remained undefined.

    Purpose of the Study:

    • To investigate the intrinsic enzymatic activity of purified ubiquitin.
    • To characterize the proteolytic properties of ubiquitin.
    • To explore the potential role of ubiquitin's protease activity in cellular regulation.

    Main Methods:

    • Purification of ubiquitin.
    • Assay of proteolytic activity using purified ubiquitin.
    • Inhibition studies using monoclonal antibodies, Ca2+, and protease inhibitors (PMSF, DFP).

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  • Analysis of protein cleavage sites.

    • Main Results:

    • Purified ubiquitin exhibits intrinsic proteolytic activity comparable to known proteases.
    • This activity occurs over a broad pH range, optimal at pH 8.0.
    • Activity is stimulated by Ca2+ and inhibited by PMSF and DFP.
    • Ubiquitin cleaves proteins at specific, limited sites.

    Conclusions:

    • Ubiquitin possesses inherent protease activity.
    • Ubiquitination may convert a protein into a specific protease.
    • This mechanism could regulate diverse cellular events.